Research workbench
Mamm ctd H264E-E289H
Analyse Mamm ctd H264E-E289H in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HAN
- Type
- protein
- Length
- 355 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q6NE57
- Ligands
- SO4, CL
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 94 | — | Q6NE57 |
| B | — | protein | 84 | — | Q6NE57 |
| C | — | protein | 95 | — | Q6NE57 |
| D | — | protein | 82 | — | Q6NE57 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · chains A
- BME · Beta-mercaptoethanol · additive · 4 copies · chains B, A, C, D
- 1PE · Pentaethylene glycol · additive · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6HAN · MamM CTD H264E-E289H · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q6NE57
- Elsewhere: RCSB PDB 6HAN · PDBe 6HAN · UniProt Q6NE57
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